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Adrenomedullin (AM) is comprised of 52 amino acids and was originally isolated in pheochromocytoma tissue by its ability to elevate cAMP in rat platelets. It is now recognized as a potent circulating vasodilatory peptide which is secreted by ubiquitous cells and organs [1]. Because the cytoprotective effect of AM is mediated by the cAMP signaling pathway, it is expected that AM is involved in various cellular processes [2]. Circulating AM is mainly secreted from vascular endothelial and smooth muscle cells. AM is processed from its

precursor as the intermediate form. Subsequently, the intermediate form is converted by enzymatic amidation [3] to the biologically active next mature form of AM (mAM). Since AM is biologically active only after C-terminal amidation of immature AM, it is necessary to determine the level of mAM in order to investigate the pathological role of AM [4]. It has also been reported that hyperglycemia enhances AM expression in the vessels, indicating that AM is involved in the regulation of glycemic PF-01367338 molecular weight control [5]. Plasma AM concentration in diabetic patients is closely associated with diabetic vascular complications [6]. However, only limited information on mAM level or amidation activity is available. Generally, the dialysate used in peritoneal dialysis (PD) has a high glucose concentration of 1.5–2.5 %; this high glucose concentration leads to deterioration of the peritoneum.

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